Department of Chemistry

Xavier University of Louisiana

Heather R Williamson, PhD.
Assistant Professor

Telephone Number: (504) 520 - 7372
Room Number: NCF Annex - Room 301H
Email Address:



Introduction to Biochemistry (3130), Introduction to Biochemistry Lab (3130L), General Chemistry 1 Lab (1011L)

Short Professional Biography

Dr. Williamson received her B.S. degree in Chemistry from the University of Alabama at Birmingham in 2006. She then went on to California Institute of Technology where she worked with Professor Harry B Gray on designing multi-step electron transfer (hopping) in engineered protein systems defending her thesis in 2012. Dr. Williamson then went on to do a postdoc with Professor Carrie Wilmot at the University of Minnesota in order to expand her skills in structural biology by focusing on identifying oxidative damage in a diheme enzyme, MauG, due to its auto-reduction of the catalytic high-valent iron species. (2012-2013) In order to expand her biochemical background in enzymology and biophysical techniques, Dr. Williamson continued her postdoctoral work with a collaborator Professor Victor Davidson at University of Central Florida. There Dr. Williamson was able to focus on how MauG’s structure regulates the mechanism of heme auto-reduction. (2013-2016) Dr. Williamson joined the Chemistry faculty at Xavier University of Louisiana in August 2016.

Research Interest

Dr. Williamson’s research is focused on potent biological oxidants, high-valent iron heme species, and the biophysical and structural properties of heme proteins that regulate the reduction of the high-valent state. When high-valent heme reduction is mis-regulated in the body, biologically detrimental oxidations occur within the protein and to non-native substrates. Certain substrates such as low density lipoproteins (LDLs), once oxidized, have been implicated in the disease pathology of heart disease. Dr. Williamson is focusing on three human heme proteins, myeloperoxidase, hemoglobin, and myoglobin. By studying the kinetic mechanism of their high-valent heme reduction, Dr. Williamson will explore structural features of the protein which tune electron and proton transfer during reduction.

Current Grant Support


Recent Publications

Sehanobish E, Williamson HR, Davidson VL. Roles of conserved residues of GoxA in controlling glycine oxidase activity, cooperativity, subunit composition and cysteine tryptophylquinone biosythensis. J Bio Chem. 2016. jbc.M116.741835.

Ma Z, Williamson HR, Davidson VL. A suicide mutation affecting proton transfers to high-valent hemes causes inactivation of MauG during catalysis. Biochemistry. 2016; 55(40):5738-5745.

Ma Z, Williamson HR, Davidson VL. Mechanisms of protein oxidative damage that is coupled to long-range electron transfer to high-valent hemes. Biochemical Journal. 2016; 473(12).

Sehanobish E, Camprillo-Brocal JC, Williamson HR, Sanchez-Amat A, Davidson VL. Interactions of GoxA with its modifying enzyme and its subunit assembly are dependent on the exten of cysteine tryptophylquinone biosynthesis. Biochemisty. 2016; 55(16): 2305-2308.

Ma Z*, Williamson HR*, Davidson VL. Roles of multiple-proton transfer pathways and proton-coupled electron transfer in the reactivity of the bis-FeIV state of MauG. Proc Natl Acad Sci U S A. 2015; 112(35):10896-901.

Williamson HR, Dow BA, Davidson VL. Mechanisms for control of biological electron transfer reactions. Bioorganic chemistry. 2014; 57:213-21.

Yukl ET, Williamson HR, Higgins L, Davidson VL, Wilmot CM. Oxidative damage in MauG: implications for the control of high-valent iron species and radical propagation pathways. Biochemistry. 2013;52(52):9447-55

Takematsu K*, Williamson H*, Blanco-Rodriguez AM, Sokolova L, Vlcek A Jr, Gray HB et al. Tryptophan-accelerated electron flow across a protein-protein interface. J Am Chem Soc. 2013; 135(41):15515-25.

Sokolova L, Williamson H, Gray HB, Vlcek A Jr, et al. Mass spectrometric characterization of oligomers in Pseudomonas aeruginosa azurin solutions. J Phys Chem B. 2011; 115(16):4790-800.

Department of Chemistry